ID   OLED_SHEON              Reviewed;         387 AA.
AC   Q8EG63;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=2-alkyl-3-oxoalkanoate reductase {ECO:0000305};
DE            EC=1.1.1.412 {ECO:0000250|UniProtKB:B2FI29};
GN   Name=oleD {ECO:0000303|PubMed:20418444};
GN   OrderedLocusNames=SO_1745 {ECO:0000312|EMBL:AAN54799.1};
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
RN   [2]
RP   FUNCTION IN OLEFIN BIOSYNTHESIS, AND DISRUPTION PHENOTYPE.
RC   STRAIN=MR-1;
RX   PubMed=20418444; DOI=10.1128/aem.00433-10;
RA   Sukovich D.J., Seffernick J.L., Richman J.E., Hunt K.A., Gralnick J.A.,
RA   Wackett L.P.;
RT   "Structure, function, and insights into the biosynthesis of a head-to-head
RT   hydrocarbon in Shewanella oneidensis strain MR-1.";
RL   Appl. Environ. Microbiol. 76:3842-3849(2010).
CC   -!- FUNCTION: Involved in olefin biosynthesis (PubMed:20418444). Catalyzes
CC       the reversible stereospecific NADPH-dependent reduction of 2-alkyl-3-
CC       oxoalkanoic acids to 2-alkyl-3-hydroxyalkanoic acids (By similarity).
CC       The S.oneidensis oleABCD genes produce 3,6,9,12,15,19,22,25,28-
CC       hentriacontanonaene, which may aid the cells in adapting to a sudden
CC       drop in temperature (PubMed:20418444). {ECO:0000250|UniProtKB:B2FI29,
CC       ECO:0000269|PubMed:20418444}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (2R,3S)-2-alkyl-3-hydroxyalkanoate + NADP(+) = an (R)-2-
CC         alkyl-3-oxoalkanoate + H(+) + NADPH; Xref=Rhea:RHEA:54796,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:138340, ChEBI:CHEBI:138341; EC=1.1.1.412;
CC         Evidence={ECO:0000250|UniProtKB:B2FI29};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54798;
CC         Evidence={ECO:0000250|UniProtKB:B2FI29};
CC   -!- DISRUPTION PHENOTYPE: Deletion of the entire oleABCD gene cluster leads
CC       to the complete absence of nonpolar extractable products. The oleABCD
CC       deletion strain shows a significantly longer lag phase than the wild-
CC       type strain when shifted to a lower temperature.
CC       {ECO:0000269|PubMed:20418444}.
CC   -!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
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DR   EMBL; AE014299; AAN54799.1; -; Genomic_DNA.
DR   RefSeq; NP_717355.1; NC_004347.2.
DR   AlphaFoldDB; Q8EG63; -.
DR   SMR; Q8EG63; -.
DR   STRING; 211586.SO_1745; -.
DR   PaxDb; Q8EG63; -.
DR   KEGG; son:SO_1745; -.
DR   PATRIC; fig|1028802.3.peg.1160; -.
DR   eggNOG; COG0451; Bacteria.
DR   HOGENOM; CLU_007383_6_1_6; -.
DR   OMA; WGPGDTQ; -.
DR   OrthoDB; 1928091at2; -.
DR   PhylomeDB; Q8EG63; -.
DR   BioCyc; MetaCyc:MON-17300; -.
DR   BioCyc; SONE211586:G1GMP-1600-MON; -.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01073; 3Beta_HSD; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..387
FT                   /note="2-alkyl-3-oxoalkanoate reductase"
FT                   /id="PRO_0000446918"
FT   ACT_SITE        190
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:B2FI29"
FT   BINDING         194
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:B2FI29"
SQ   SEQUENCE   387 AA;  41885 MW;  987431C558BC1423 CRC64;
     MTDNSSISLT PADLEHVPLQ PTRLKQVGGD QACIKLSLDA REQTALDALA AKVSHAFVTG
     AGGFLGKAIC QRLIAAGIKV TGFARGRYLE LEALGVTMVQ GDLVNPEQVK QAMQGCDIVF
     HVASKAGVWG DRDSYFCPNV KGAANVIAAC KALKINKLVY TSTPSVTFAG EDESGINEST
     PYASRFLNYY AHSKAIAEKM MLDANQSSST NAAYVLKTVA LRPHLIWGPN DPHLVPRVLA
     RGRLGKLKLV GREDKLVDTI YIDNAAYAHV LAALELCQAT PKCQGKAYFI SNDEPVTMAK
     MLNMILACDG LPPVTQRVPQ MLAYAVGAVL ETAYRLLNKQ EEPIMTRFVA KQLSCSHYFD
     ISAAKQDFGY SALVSIEEGM KRLKASL